The common severe Z mutation (E342K) of α1-antitrypsin forms intracellular polymers that are associated with liver cirrhosis. The native fold of this protein is well-established and models have been proposed from crystallographic and biophysical data for the stable inter-molecular configuration that terminates the polymerisation pathway. Despite these molecular 'snapshots', the details of the transition between monomer and polymer remain only partially understood. We surveyed the reactive centre loop of α1-antitrypsin to identify sites important for progression, through intermediate states, to polymer. Mutations at P14P12 and P4, but not P10P8 or P2P1', resulted in a decrease in detectable polymer in a cell model that recapitulates the intr...
AbstractThe human serine protease inhibitor (serpin) α-1 antitrypsin (α1-AT) protects tissues from p...
AbstractAlpha1-antitrypsin deficiency results from point mutations that distort the structure of the...
Conformational diseases are caused by a structural rearrangement within a protein that results in ab...
The common severe Z mutation (E342K) of α1-antitrypsin forms intracellular polymers that are associa...
The common severe Z mutation (E342K) of alpha(1)-antitrypsin forms intracellular polymers that are a...
The formation of ordered Z (Glu342Lys) α1 -antitrypsin polymers in hepatocytes is central to liver d...
Protease inhibitors of the serpin family are characterised by a metastable native fold which is nece...
α1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pulmonary ...
α1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pulmonary ...
Abstractα1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pu...
AbstractThe common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that ...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
α1-Antitrypsin is an abundant plasma inhibitor of neutrophil elastase,expressed at high levels by he...
α1-Antitrypsin (α1AT) deficiency, the most common serpinopathy, results in both emphysema and liver ...
AbstractThe human serine protease inhibitor (serpin) α-1 antitrypsin (α1-AT) protects tissues from p...
AbstractAlpha1-antitrypsin deficiency results from point mutations that distort the structure of the...
Conformational diseases are caused by a structural rearrangement within a protein that results in ab...
The common severe Z mutation (E342K) of α1-antitrypsin forms intracellular polymers that are associa...
The common severe Z mutation (E342K) of alpha(1)-antitrypsin forms intracellular polymers that are a...
The formation of ordered Z (Glu342Lys) α1 -antitrypsin polymers in hepatocytes is central to liver d...
Protease inhibitors of the serpin family are characterised by a metastable native fold which is nece...
α1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pulmonary ...
α1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pulmonary ...
Abstractα1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pu...
AbstractThe common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that ...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
α1-Antitrypsin is an abundant plasma inhibitor of neutrophil elastase,expressed at high levels by he...
α1-Antitrypsin (α1AT) deficiency, the most common serpinopathy, results in both emphysema and liver ...
AbstractThe human serine protease inhibitor (serpin) α-1 antitrypsin (α1-AT) protects tissues from p...
AbstractAlpha1-antitrypsin deficiency results from point mutations that distort the structure of the...
Conformational diseases are caused by a structural rearrangement within a protein that results in ab...